Purification and characterization of antioxidant peptides of Pseudosciaena crocea protein hydrolysates

Abstract

Two peptides with antioxidant activity were isolated from Pseudosciaena crocea proteins. Pseudosciaena crocea muscle was hydrolyzed with neutral protease to obtain Pseudosciaena crocea protein hydrolysates (PCPH). After ultrafiltration through molecular weight cut-off membranes of 10, 5 and 3 kDa and assessment of free radical scavenging ability, the fraction (PCPH-IV) with the highest antioxidant activity was obtained. Several purification steps, i.e., ion exchange chromatography, gel filtration chromatography and reversed phase high performance liquid chromatography, were applied to further purify PCPH-IV. Two antioxidant peptides with the amino acid sequences Ser-Arg-Cys-His-Val and Pro-Glu-His-Trp were finally identified by LC-MS/MS.